NFYA_MOUSE
ID NFYA_MOUSE Reviewed; 346 AA.
AC P23708;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Nuclear transcription factor Y subunit alpha;
DE AltName: Full=CAAT box DNA-binding protein subunit A;
DE AltName: Full=Nuclear transcription factor Y subunit A;
DE Short=NF-YA;
GN Name=Nfya;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1549471; DOI=10.1093/nar/20.5.1087;
RA Li X.-Y., Mantovani R., Hooft van Huijsduijnen R., Andre I., Benoist C.,
RA Mathis D.;
RT "Evolutionary variation of the CCAAT-binding transcription factor NF-Y.";
RL Nucleic Acids Res. 20:1087-1091(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1577736; DOI=10.1016/s0021-9258(19)50377-5;
RA Li X.-Y., Hooft van Huijsduijnen R., Mantovani R., Benoist C.O., Mathis D.;
RT "Intron-exon organization of the NF-Y genes. Tissue-specific splicing
RT modifies an activation domain.";
RL J. Biol. Chem. 267:8984-8990(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-25 AND 54-346, AND PARTIAL PROTEIN
RP SEQUENCE.
RX PubMed=1698608;
RA Hooft van Huijsduijnen R., Li X.-Y., Black D., Matthes H., Benoist C.,
RA Mathis D.;
RT "Co-evolution from yeast to mouse: cDNA cloning of the two NF-Y (CP-1/CBF)
RT subunits.";
RL EMBO J. 9:3119-3127(1990).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION.
RX PubMed=24030830; DOI=10.1074/jbc.m113.507038;
RA Xiao J., Zhou Y., Lai H., Lei S., Chi L.H., Mo X.;
RT "Transcription factor NF-Y is a functional regulator of the transcription
RT of core clock gene Bmal1.";
RL J. Biol. Chem. 288:31930-31936(2013).
CC -!- FUNCTION: Component of the sequence-specific heterotrimeric
CC transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3'
CC box motif found in the promoters of its target genes. NF-Y can function
CC as both an activator and a repressor, depending on its interacting
CC cofactors. NF-YA positively regulates the transcription of the core
CC clock component ARNTL/BMAL1. {ECO:0000269|PubMed:24030830}.
CC -!- SUBUNIT: Heterotrimeric transcription factor composed of three
CC components, NF-YA, NF-YB and NF-YC. NF-YB and NF-YC must interact and
CC dimerize for NF-YA association and DNA binding (By similarity).
CC Interacts with SP1; the interaction is inhibited by glycosylation of
CC SP1. Interacts (via N-terminus) with ZHX2 (via homeobox domain).
CC Interacts with ZFX3. Interacts with ZHX1 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P23708; P08047: SP1; Xeno; NbExp=18; IntAct=EBI-862337, EBI-298336;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P23708-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P23708-2; Sequence=VSP_000850;
CC -!- SIMILARITY: Belongs to the NFYA/HAP2 subunit family.
CC {ECO:0000255|PROSITE-ProRule:PRU00966}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X55315; CAA39023.1; -; mRNA.
DR EMBL; M86215; AAA39817.1; -; mRNA.
DR EMBL; M86214; AAA39816.1; -; mRNA.
DR CCDS; CCDS28867.1; -. [P23708-2]
DR CCDS; CCDS84321.1; -. [P23708-1]
DR PIR; A38245; A38245.
DR PIR; C38245; C38245.
DR PIR; D38245; D38245.
DR PIR; E38245; E38245.
DR RefSeq; NP_001334330.1; NM_001347401.1. [P23708-1]
DR RefSeq; NP_001334331.1; NM_001347402.1.
DR RefSeq; NP_035043.1; NM_010913.2. [P23708-2]
DR AlphaFoldDB; P23708; -.
DR SMR; P23708; -.
DR BioGRID; 201760; 17.
DR ComplexPortal; CPX-89; CCAAT-binding factor complex.
DR CORUM; P23708; -.
DR DIP; DIP-2661N; -.
DR IntAct; P23708; 15.
DR MINT; P23708; -.
DR STRING; 10090.ENSMUSP00000043909; -.
DR iPTMnet; P23708; -.
DR PhosphoSitePlus; P23708; -.
DR EPD; P23708; -.
DR jPOST; P23708; -.
DR MaxQB; P23708; -.
DR PaxDb; P23708; -.
DR PRIDE; P23708; -.
DR ProteomicsDB; 252830; -. [P23708-1]
DR ProteomicsDB; 252831; -. [P23708-2]
DR Antibodypedia; 3982; 233 antibodies from 35 providers.
DR DNASU; 18044; -.
DR Ensembl; ENSMUST00000078800; ENSMUSP00000077853; ENSMUSG00000023994. [P23708-1]
DR Ensembl; ENSMUST00000162460; ENSMUSP00000123785; ENSMUSG00000023994. [P23708-2]
DR GeneID; 18044; -.
DR KEGG; mmu:18044; -.
DR UCSC; uc008cxp.2; mouse. [P23708-1]
DR CTD; 4800; -.
DR MGI; MGI:97316; Nfya.
DR VEuPathDB; HostDB:ENSMUSG00000023994; -.
DR eggNOG; KOG1561; Eukaryota.
DR GeneTree; ENSGT00390000015714; -.
DR InParanoid; P23708; -.
DR OMA; GNMMNSG; -.
DR PhylomeDB; P23708; -.
DR BioGRID-ORCS; 18044; 8 hits in 75 CRISPR screens.
DR ChiTaRS; Nfya; mouse.
DR PRO; PR:P23708; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P23708; protein.
DR Bgee; ENSMUSG00000023994; Expressed in secondary oocyte and 82 other tissues.
DR ExpressionAtlas; P23708; baseline and differential.
DR Genevisible; P23708; MM.
DR GO; GO:0016602; C:CCAAT-binding factor complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IGI:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:MGI.
DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0035065; P:regulation of histone acetylation; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR InterPro; IPR018362; CCAAT-binding_factor_CS.
DR InterPro; IPR001289; NFYA.
DR PANTHER; PTHR12632; PTHR12632; 1.
DR Pfam; PF02045; CBFB_NFYA; 1.
DR PRINTS; PR00616; CCAATSUBUNTB.
DR SMART; SM00521; CBF; 1.
DR PROSITE; PS00686; NFYA_HAP2_1; 1.
DR PROSITE; PS51152; NFYA_HAP2_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Biological rhythms;
KW Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..346
FT /note="Nuclear transcription factor Y subunit alpha"
FT /id="PRO_0000198769"
FT DNA_BIND 295..320
FT /note="NFYA/HAP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00966"
FT REGION 298..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 265..288
FT /note="Subunit association domain (SAD)"
FT COMPBIAS 311..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 26..53
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_000850"
FT CONFLICT 182..187
FT /note="Missing (in Ref. 2; AAA39816)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 36779 MW; 1291AA0D3AA76E05 CRC64;
MEQYTTNSNS STEQIVVQAG QIQQQQGGVT AVQLQTEAQV ASASGQQVQT LQVVQGQPLM
VQVSGGQLIT STGQPIMVQA VPGGQGQTIM QVPVSGTQGL QQIQLVPPGQ IQIQGGQAVQ
VQGQQGQTQQ IIIQQPQTAV TAGQTQTQQQ IAVQGQQVAQ TAEGQTIVYQ PVNADGTILQ
QVTVPVSGMI TIPAASLAGA QIVQTGANTN TTSSGQGTVT VTLPVAGNVV NSGGMVMMVP
GAGSVPAIQR IPLPGAEMLE EEPLYVNAKQ YHRILKRRQA RAKLEAEGKI PKERRKYLHE
SRHRHAMARK RGEGGRFFSP KEKDSPHMQD PNQADEEAMT QIIRVS
